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  • 1.
    Ahmadi, Mazaher
    et al.
    Bu Ali Sina Univ, Fac Chem, Hamadan, Iran..
    Moein, Mohammad Mahdi
    Karolinska Inst, Ctr Psychiat Res, Dept Clin Neurosci, SE-17176 Stockholm, Sweden.;Stockholm Cty Council, SE-17176 Stockholm, Sweden..
    Madrakian, Tayyebeh
    Bu Ali Sina Univ, Fac Chem, Hamadan, Iran..
    Afkhami, Abbas
    Bu Ali Sina Univ, Fac Chem, Hamadan, Iran..
    Bahar, Soleiman
    Univ Kurdistan, Fac Sci, Dept Chem, Sanandaj, Iran..
    Abdel-Rehim, Mohamed
    KTH, School of Engineering Sciences (SCI), Applied Physics, Materials and Nanophysics. Karolinska Inst, Ctr Psychiat Res, Dept Clin Neurosci, SE-17176 Stockholm, Sweden.;Stockholm Cty Council, SE-17176 Stockholm, Sweden..
    Reduced graphene oxide as an efficient sorbent in microextraction by packed sorbent: Determination of local anesthetics in human plasma and saliva samples utilizing liquid chromatography-tandem mass spectrometry2018In: Journal of chromatography. B, ISSN 1570-0232, E-ISSN 1873-376X, Vol. 1095, p. 177-182Article in journal (Refereed)
    Abstract [en]

    Herein, reduced graphene oxide (RGO) has been utilized as an efficient sorbent in microextraction by packed sorbent (MEPS). The combination of MEPS and liquid chromatography-tandem mass spectrometry has been used to develop a method for the extraction and determination of three local anesthetics (i.e. lidocaine, prilocaine, and ropivacaine) in human plasma and saliva samples. The results showed that the utilization of RGO in MEPS could minimize the matrix effect so that no interfering peaks at the retention times of the analytes or internal standard was observed. The high extraction efficiency of this method was approved by mean recoveries of 97.26-106.83% and 95.21-105.83% for the studied analytes in plasma and saliva samples, respectively. Intra- and inter-day accuracies and precisions for all analytes were in good accordance with the international regulations. The accuracy values (as percentage deviation from the nominal value) of the quality control samples were between - 2.1 to 13.9 for lidocaine, - 4.2 to 11.0 for prilocaine and between - 4.5 to - 2.4 for ropivacaine in plasma samples while the values were ranged from - 4.6 to 1.6 for lidocaine, from - 4.2 to 15.5 for prilocaine and from - 3.3 to - 2.3 for ropivacaine in human saliva samples. Lower and upper limit of quantification (LLOQ, ULOQ) were set at 5 and 2000 nmol L-1 for all of the studied drugs. The correlation coefficients values were >= 0.995. The limit of detection values were obtained 4 nmol L-1 for lidocaine and prilocaine, and 2 nmol L-1 for ropivacaine.

  • 2.
    Boström, Tove
    et al.
    KTH, School of Biotechnology (BIO), Protein Technology.
    Ottosson Takanen, Jenny
    KTH, School of Biotechnology (BIO), Proteomics and Nanobiotechnology.
    Hober, Sophia
    KTH, School of Biotechnology (BIO), Protein Technology.
    Antibodies as means for selective mass spectrometry2015In: Journal of chromatography. B, ISSN 1570-0232, E-ISSN 1873-376XArticle in journal (Refereed)
    Abstract [en]

    For protein analysis of biological samples, two major strategies are used today; mass spectrometry (MS) and antibody-based methods. Each strategy offers advantages and drawbacks. However, combining the two using an immunoenrichment step with MS analysis brings together the benefits of each method resulting in increased sensitivity, faster analysis and possibility of higher degrees of multiplexing. The immunoenrichment can be performed either on protein or peptide level and quantification standards can be added in order to enable determination of the absolute protein concentration in the sample. The combination of immunoenrichment and MS holds great promise for the future in both proteomics and clinical diagnostics. This review describes different setups of immunoenrichment coupled to mass spectrometry and how these can be utilized in various applications.

  • 3.
    Hober, Sophia
    et al.
    KTH, School of Biotechnology (BIO), Proteomics (closed 20130101).
    Nord, Karin
    Linhult, Martin
    Protein A chromatography for antibody purification2007In: Journal of chromatography. B, ISSN 1570-0232, E-ISSN 1873-376X, Vol. 848, no 1, p. 40-47Article, review/survey (Refereed)
    Abstract [en]

    Staphylococcal protein A (SPA) is one of the first discovered immunoglobulin binding molecules and has been extensively studied during the past decades. Due to its affinity to immunoglobulins, SPA has found widespread use as a tool in the detection and purification of antibodies and the molecule has been further developed to one of the most employed affinity purification systems. Interestingly, a minimized SPA derivative has been constructed and a domain originating from SPA has been improved to withstand the harsh environment employed in industrial purifications. This review will focus on the development of different affinity molecules and matrices for usage in antibody purification.

  • 4.
    Jacksén, Johan
    et al.
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Analytical Chemistry.
    Dahl, Kenneth
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Analytical Chemistry.
    Karlberg, Ann-Therese
    Redeby, Theres
    Emmer, Åsa
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Analytical Chemistry.
    Capillary electrophoresis separation and matrix-assisted laser desorption/ionization mass spectrometry characterization of bovine serum albumin fluorescein isothiocyanate conjugates2010In: Journal of chromatography. B, ISSN 1570-0232, E-ISSN 1873-376X, Vol. 878, no 15-16, p. 1125-1134Article in journal (Refereed)
    Abstract [en]

    A protocol using enzymatic digestion, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) and capillary electrophoresis with laser induced fluorescence detection (CE-LIF) for the investigation of the binding of the fluorescent contact allergen fluorescein isothiocyanate (FITC) to the 66 kDa large protein bovine serum albumin (BSA), as a model system for protein-hapten binding in the skin, is presented. Mass spectra of BSA-FITC digestions, using trypsin and chymotrypsin, respectively, provided sequence coverage of 97%. To investigate the number of FITC-bound peptides using CE-LIF separation, three different buffer salts at four different pH levels were evaluated. The use of 20 mM sodium citrate pH 6.5 as well as 20 mM sodium phosphate pH 6.5 or pH 7.5 as background electrolyte revealed high numbers of peptides with at least one bound FITC. The effect of the electrolyte counter ion on MALDI-MS was investigated and was found to have effect on the MALDI spectra signal-to-noise (S/N) at 50 mM but not at 10 m M. Of the 60 theoretical FITC-binding sites in BSA this MALDI-MS protocol presents 30 defined. 28 possible and 2 non-binding sites for FITC. (C) 2010 Elsevier B.V. All rights reserved.

  • 5.
    Romson, Joakim
    et al.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Applied Physical Chemistry.
    Jacksen, Johan
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Applied Physical Chemistry. Biotage Sweden AB, Uppsala, Sweden..
    Emmer, Åsa
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Applied Physical Chemistry.
    An automated system for CE-MALDI and on-target digestion under a fluorocarbon lid applied on spermatophore proteins from Pieris napi2019In: Journal of chromatography. B, ISSN 1570-0232, E-ISSN 1873-376X, Vol. 1104, p. 228-233Article in journal (Refereed)
    Abstract [en]

    A method for off-line CE-MALDI-TOF-MS and MS2, and on-target digestion under a fluorocarbon lid was developed and applied for the analysis of proteins in the spermatophore of the butterfly Pieris napi. Fractionation revealed many peptides otherwise not detected or resolved. Automated fractionation was performed with an in-lab developed robotic system, and automated on-target tryptic digestion under a fluorocarbon lid was demonstrated with the same system. Fractionation onto a pre-structured MALDI-concentration plate facilitated aligned deposition of trypsin and MALDI-matrix with the deposited sample, also under the fluorocarbon lid. Some indications of indigenous proteolysis of spermatophore proteins were seen, and searching MS2 spectra suggested three tentative sequence homologies to P. rapae. The study demonstrates the functionality of the lab-made robot. Detailed manufacturing instructions and code are provided. The feasibility of automated on-target digestion under a fluorocarbon lid, and the usefulness of a structured concentration plate in CE-MALDI fractionation was shown. Further, it constitutes a preliminary study of P. napi spermatophore proteins.

  • 6.
    Romson, Joakim
    et al.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Organic chemistry.
    Jacksén, Johan
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry.
    Emmer, Åsa
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Applied Physical Chemistry.
    An automated system for CE-MALDI and on-target digestion under a fluorocarbon lid applied on spermatophore proteins from Pieris napiIn: Journal of chromatography. B, ISSN 1570-0232, E-ISSN 1873-376XArticle in journal (Refereed)
    Abstract [en]

    A method for off-line CE‑MALDI‑TOF-MS and MS2, and on-target digestion under a fluorocarbon lid was developed and applied for the analysis of proteins in the spermatophore of the butterfly Pieris napi. Fractionation revealed many peptides otherwise not detected or resolved. Automated fractionation was performed with an in-lab developed robotic system, and automated on-target tryptic digestion under a fluorocarbon lid was demonstrated with the same system. Fractionation onto a pre-structured MALDI-concentration plate facilitated aligned deposition of trypsin and MALDI-matrix with the deposited sample, also under the fluorocarbon lid. Some indications of indigenous proteolysis of spermatophore proteins were seen, and searching MS2 spectra suggested three tentative sequence homologies to P. rapae. The study demonstrates the functionality of the lab-made robot. Detailed manufacturing instructions and code are provided. The feasibility of automated on-target digestion under a fluorocarbon lid, and the usefulness of a structured concentration plate in CE-MALDI fractionation was shown. Further, it constitutes a preliminary study of P. napi spermatophore proteins.

  • 7. Soultani-Vigneron, S.
    et al.
    Dugas, V.
    Rouillat, M. H.
    Fedolliere, J.
    Duclos, M. C.
    Vnuk, E.
    Phaner-Goutorbe, M.
    Bulone, Vincent
    KTH, School of Biotechnology (BIO), Glycoscience.
    Martin, J. R.
    Wallach, J.
    Cloarec, J. P.
    Immobilisation of oligo-peptidic probes for microarray implementation: Characterisation by FTIR, Atomic Force Microscopy and 2D fluorescence2005In: Journal of chromatography. B, ISSN 1570-0232, E-ISSN 1873-376X, Vol. 822, no 02-jan, p. 304-310Article in journal (Refereed)
    Abstract [en]

    Proteomic microarrays show a wide range of applications for the investigation of DNA-protein, enzyme-substrate as well as protein-protein interactions. Among many challenges to build a viable protein microarray, the surface chemistry that will allow to immobilised various proteins to retain their biological activity is of paramount importance. Here we report a chemical functionalisation method allowing immobilisation of oligo-peptides onto silica surface (porous silica, glass, thermal silicon dioxide). Substrates were first derivatised with a monofunctional silane allowing the elaboration of dense and uniform monolayers in highly reproducible way. Prior to the oligo-peptides grafting, this organic layer was functionalised with an amino-polyethyleneglycol. The coupling step of oligo-peptides onto functionalised supports is achieved through activation of the C-terminal function of the oligo-peptides. Chemical surface modifications were followed by FTIR spectroscopy, AFM measurements and fluorescence scanning microscopy. A systematic study of the oligo-peptide grafting conditions (time, concentration, solvent) was carried out to optimise this step. The oligo-peptides grafting strategy implemented in this work ensure a covalent and oriented grafting of the oligo-peptides. This orientation is ensured through the use of fully protected peptide except the terminal primary an-tine. The immobilized peptides will be then deprotected before biological recognition. This strategy is crucial to retain the biological activity of thousands of oligo-probes assessed on a microarray.

  • 8.
    Sundqvist, Gustav
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience.
    Stenvall, Maria
    KTH, School of Biotechnology (BIO).
    Berglund, Helena
    Ottosson, Jenny
    KTH, School of Biotechnology (BIO).
    Brumer, Harry
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Biotechnology (BIO), Centres, Albanova VinnExcellence Center for Protein Technology, ProNova.
    A general, robust method for the quality control of intact proteins using LC–ESI-MS2007In: Journal of chromatography. B, ISSN 1570-0232, E-ISSN 1873-376X, Vol. 852, no 1-2, p. 188-194Article in journal (Refereed)
    Abstract [en]

    A simple and robust method for the routine quality control of intact proteins based on liquid chromatography coupled to electrospray ionization mass spectrometry (LC-ESI-MS) is presented. A wide range of prokaryotic and eukaryotic proteins expressed recombinantly in Escherichia coli or Pichia pastoris has been analyzed with medium- to high-throughput with on-line desalting from multi-well sample plates. Particular advantages of the method include fast chromatography and short cycle times, the use of inexpensive trapping/desalting columns, low sample carryover, and the ability to analyze proteins with masses ranging from 5 to 100 kDa with greater than 50 ppm accuracy. Moreover, the method can be readily coupled with optimized chemical reduction and alkylation steps to facilitate the analysis of denatured or incorrectly folded proteins (e.g., recombinant proteins sequestered in E. coli inclusion bodies) bearing cysteine residues, which otherwise form intractable multimers and non-specific adducts by disulfide bond formation.

  • 9. Syren, Per-Olof
    et al.
    Rozkov, Aleksei
    Schmidt, Stefan R.
    Stroemberg, Patrik
    Milligram scale parallel purification of plasmid DNA using anion-exchange membrane capsules and a multi-channel peristaltic pump2007In: Journal of chromatography. B, ISSN 1570-0232, E-ISSN 1873-376X, Vol. 856, p. 68-74Article in journal (Refereed)
    Abstract [en]

    A parallel chromatog. procedure for the purifn. of milligram amts. of plasmid DNA was developed. Initial studies showed that ion-exchange membrane capsules displayed high capacity for plasmid DNA. Interestingly, a weak anion exchanger (DEAE) proved to be superior to the strong quaternary ammonium group with respect to elution and regeneration properties and the 75 cm2 Sartobind D membrane capsule (MA75D, Sartorius) was selected for further studies. A method for reducing endotoxin levels by using CTAB as a precipitant was optimized. By introducing this step into the protocol, endotoxin levels could be reduced approx. 100-fold to ≤5 EU/mg plasmid. The parallel procedure was set up on a multi-channel peristaltic pump and evaluated with four different vectors (2.7-11.5 kbp). Starting with 5-10 g of E. coli cell paste (wet wt.) generally satd. the membrane adsorber, resulting in plasmid DNA yields close to 10 mg. [on SciFinder(R)]

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